2OX2
Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles
Summary for 2OX2
| Entry DOI | 10.2210/pdb2ox2/pdb |
| Related | 1qvk 1qvl 1ski 1skk 1skl 2otq |
| Descriptor | cRW2 peptide (1 entity in total) |
| Functional Keywords | antimicrobial, cationic peptide, antimicrobial protein |
| Total number of polymer chains | 1 |
| Total formula weight | 1009.19 |
| Authors | Appelt, C.,Wessolowski, A.,Soderhall, J.A.,Dathe, M.,Schmieder, P. (deposition date: 2007-02-19, release date: 2007-12-25, Last modification date: 2022-03-16) |
| Primary citation | Appelt, C.,Wessolowski, A.,Dathe, M.,Schmieder, P. Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity. J.Pept.Sci., 14:524-527, 2007 Cited by PubMed Abstract: New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides. PubMed: 17985394DOI: 10.1002/psc.924 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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